膜蛋白的电子显微镜和原子力显微镜观察

Electron and atomic force microscopy of membrane proteins.

作者信息

Heymann J B, Müller D J, Mitsuoka K, Engel A

机构信息

ME Müller-Institute for Microscopic Structural Biology at the Biozentrum, University of Basel, Switzerland.

出版信息

Curr Opin Struct Biol. 1997 Aug;7(4):543-9. doi: 10.1016/s0959-440x(97)80120-0.

DOI:10.1016/s0959-440x(97)80120-0

PMID:9266177

Abstract

Electron crystallography is becoming a powerful tool for the resolution of membrane protein structures. The past year has seen the production of a bacteriorhodopsin model at 3.5 A and the structure of aquaporin 1 approaching atomic resolution. Determination of surface topographies of 2D crystals using the atomic force microscope is similarly advancing to a level that reveals submolecular details. As the latter is operated in solution, membrane proteins can be observed at work.

摘要

电子晶体学正成为解析膜蛋白结构的有力工具。过去一年里，已构建出分辨率为3.5埃的细菌视紫红质模型，水通道蛋白1的结构也接近原子分辨率。使用原子力显微镜测定二维晶体的表面形貌同样也发展到了能够揭示亚分子细节的水平。由于原子力显微镜是在溶液中操作，因此可以观察到膜蛋白的工作状态。